HEADER LIGASE 19-JUL-10 3O0A
TITLE CRYSTAL STRUCTURE OF THE WILD TYPE CP1 HYDROLITIC DOMAIN FROM AQUIFEX
TITLE 2 AEOLICUS LEUCYL-TRNA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LEUCYL-TRNA SYNTHETASE SUBUNIT ALPHA;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: HYDROLYTIC DOMAIN (UNP RESIDUES 225-443);
COMPND 5 SYNONYM: LEUCINE--TRNA LIGASE SUBUNIT ALPHA, LEURS;
COMPND 6 EC: 6.1.1.4;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: AQUIFEX AEOLICUS;
SOURCE 3 ORGANISM_TAXID: 63363;
SOURCE 4 GENE: LEUS, AQ_351;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: ROSETTA DE3;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET11C
KEYWDS AQUIFEX AEOLICUS, LEUCYL-TRNA SYNTHETASE, CP1 HYDROLYTIC DOMAIN,
KEYWDS 2 LIGASE, AMINOACYL-TRNA SYNTHETASE, ATP-BINDING, NUCLEOTIDE-BINDING,
KEYWDS 3 PROTEIN BIOSYNTHESIS
EXPDTA X-RAY DIFFRACTION
AUTHOR V.CURA,N.OLIERIC,E.-D.WANG,D.MORAS,G.ERIANI,J.CAVARELLI
REVDAT 2 06-SEP-23 3O0A 1 REMARK
REVDAT 1 17-NOV-10 3O0A 0
JRNL AUTH V.CURA,N.OLIERIC,A.GUICHARD,E.-D.WANG,D.MORAS,G.ERIANI,
JRNL AUTH 2 J.CAVARELLI
JRNL TITL CRYSTAL STRUCTURE OF THE WILD TYPE AND TWO MUTANTS OF THE
JRNL TITL 2 CP1 HYDROLYTIC DOMAIN FROM AQUIFEX AEOLICUS LEUCYL-TRNA
JRNL TITL 3 SYNTHETASE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH V.CURA,N.OLIERIC,A.GUICHARD,E.-D.WANG,D.MORAS,G.ERIANI,
REMARK 1 AUTH 2 J.CAVARELLI
REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY X-RAY CRYSTALLOGRAPHIC STUDY
REMARK 1 TITL 2 OF THE WILD TYPE AND TWO MUTANTS OF THE CP1 HYDROLYTIC
REMARK 1 TITL 3 DOMAIN FROM AQUIFEX AEOLICUS LEUCYL-TRNA SYNTHETASE
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.F V. 61 899 2005
REMARK 1 REFN ESSN 1744-3091
REMARK 1 PMID 16511190
REMARK 2
REMARK 2 RESOLUTION. 1.77 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.77
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.15
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.3
REMARK 3 NUMBER OF REFLECTIONS : 43042
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.191
REMARK 3 R VALUE (WORKING SET) : 0.188
REMARK 3 FREE R VALUE : 0.225
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.600
REMARK 3 FREE R VALUE TEST SET COUNT : 3284
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.77
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.82
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2920
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.47
REMARK 3 BIN R VALUE (WORKING SET) : 0.1910
REMARK 3 BIN FREE R VALUE SET COUNT : 242
REMARK 3 BIN FREE R VALUE : 0.2260
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3397
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 513
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.71000
REMARK 3 B22 (A**2) : 0.87000
REMARK 3 B33 (A**2) : -0.17000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.129
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.075
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.525
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.940
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.918
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3480 ; 0.009 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4710 ; 1.195 ; 1.972
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 423 ; 5.543 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 163 ;30.626 ;24.663
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 613 ;12.854 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 18 ;18.818 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 504 ; 0.078 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2650 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1734 ; 0.196 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2399 ; 0.309 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 426 ; 0.142 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 84 ; 0.248 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 42 ; 0.186 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 2163 ; 0.688 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3415 ; 1.146 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1504 ; 1.895 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1295 ; 3.040 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 228 A 438
REMARK 3 ORIGIN FOR THE GROUP (A): 19.1489 93.5933 58.6075
REMARK 3 T TENSOR
REMARK 3 T11: -0.0566 T22: -0.0591
REMARK 3 T33: -0.0415 T12: 0.0195
REMARK 3 T13: -0.0220 T23: -0.0349
REMARK 3 L TENSOR
REMARK 3 L11: 0.7108 L22: 0.7724
REMARK 3 L33: 2.2710 L12: 0.0931
REMARK 3 L13: 0.1662 L23: 0.5426
REMARK 3 S TENSOR
REMARK 3 S11: -0.0260 S12: 0.0337 S13: 0.0710
REMARK 3 S21: -0.1355 S22: -0.1265 S23: 0.0778
REMARK 3 S31: -0.1711 S32: -0.1875 S33: 0.1525
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 228 B 441
REMARK 3 ORIGIN FOR THE GROUP (A): 18.5521 73.5314 26.1530
REMARK 3 T TENSOR
REMARK 3 T11: -0.0488 T22: -0.0350
REMARK 3 T33: -0.0429 T12: -0.0234
REMARK 3 T13: -0.0095 T23: 0.0308
REMARK 3 L TENSOR
REMARK 3 L11: 0.5403 L22: 2.0719
REMARK 3 L33: 0.8836 L12: -0.0819
REMARK 3 L13: -0.1076 L23: -0.7227
REMARK 3 S TENSOR
REMARK 3 S11: -0.0101 S12: 0.0784 S13: -0.0044
REMARK 3 S21: -0.2575 S22: 0.0334 S23: 0.0818
REMARK 3 S31: 0.1360 S32: -0.0432 S33: -0.0232
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3O0A COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-JUL-10.
REMARK 100 THE DEPOSITION ID IS D_1000060502.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-MAR-05
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 8.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.934
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 43042
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.770
REMARK 200 RESOLUTION RANGE LOW (A) : 36.150
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.3
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : 0.03000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.77
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.82
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.5
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.08400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1H3N
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.97
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.1 M AMMONIUM SULFATE, 100 MM TRIS
REMARK 280 -HCL PH 8.5, 10 MM POTASSIUM CHLORIDE, 1 MM CALCIUM CHLORIDE, 1%
REMARK 280 PEG 400 FOR 30S, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 297K,
REMARK 280 PH 8.50
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 19.34450
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 58.33350
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 49.09000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 58.33350
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 19.34450
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 49.09000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A 225
REMARK 465 ARG A 226
REMARK 465 SER A 227
REMARK 465 VAL A 439
REMARK 465 SER A 440
REMARK 465 TYR A 441
REMARK 465 ARG A 442
REMARK 465 LEU A 443
REMARK 465 GLY B 225
REMARK 465 ARG B 226
REMARK 465 SER B 227
REMARK 465 ARG B 442
REMARK 465 LEU B 443
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 462 O HOH A 542 1.95
REMARK 500 O HOH A 520 O HOH B 498 2.12
REMARK 500 O HOH A 523 O HOH A 545 2.14
REMARK 500 O ASP A 327 O HOH A 573 2.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASP A 327 64.48 -178.96
REMARK 500 LYS A 328 142.97 -27.88
REMARK 500 ASP A 411 -121.20 45.78
REMARK 500 ASP B 411 -123.02 50.32
REMARK 500
REMARK 500 REMARK: NULL
DBREF 3O0A A 225 443 UNP O66680 SYLA_AQUAE 225 443
DBREF 3O0A B 225 443 UNP O66680 SYLA_AQUAE 225 443
SEQRES 1 A 219 GLY ARG SER GLU GLY ALA LEU ILE ARG PHE TYR VAL GLU
SEQRES 2 A 219 ILE GLU GLU PRO GLU LYS PHE LEU ASN CYS VAL PRO GLU
SEQRES 3 A 219 GLU LEU LYS GLU THR LEU LEU LYS GLU LYS ARG ILE TYR
SEQRES 4 A 219 ILE ASP VAL PHE THR THR ARG PRO ASP THR VAL PHE GLY
SEQRES 5 A 219 ALA THR PHE VAL VAL LEU ALA PRO GLU HIS PRO LEU VAL
SEQRES 6 A 219 PRO VAL LEU ALA CYS ILE GLY GLU ARG LEU GLY ASN ALA
SEQRES 7 A 219 CYS TYR SER ASP VAL GLU ASN PHE VAL GLU LYS MET LYS
SEQRES 8 A 219 LYS MET SER THR ARG GLU ARG THR MET GLU GLU ASP LYS
SEQRES 9 A 219 GLU GLY VAL PHE LEU GLY VAL TYR ALA THR ASN PRO ALA
SEQRES 10 A 219 ASN GLY GLU LYS ILE PRO VAL TRP SER ALA ASN TYR VAL
SEQRES 11 A 219 LEU TYR GLU TYR GLY THR GLY ALA ILE MET CYS VAL PRO
SEQRES 12 A 219 ALA HIS ASP GLN ARG ASP TRP GLU PHE ALA LYS LYS TYR
SEQRES 13 A 219 ASP LEU PRO ILE LYS VAL VAL VAL LYS PRO GLU GLY ALA
SEQRES 14 A 219 TRP ASP PHE GLU LYS GLY ALA TYR GLU GLY LYS GLY THR
SEQRES 15 A 219 LEU VAL ASN SER ASP GLY PHE ASP GLY LEU ASP SER GLU
SEQRES 16 A 219 THR ALA LYS ARG LYS ILE THR GLU TRP LEU GLN ASP ARG
SEQRES 17 A 219 GLY LEU GLY GLU LYS LYS VAL SER TYR ARG LEU
SEQRES 1 B 219 GLY ARG SER GLU GLY ALA LEU ILE ARG PHE TYR VAL GLU
SEQRES 2 B 219 ILE GLU GLU PRO GLU LYS PHE LEU ASN CYS VAL PRO GLU
SEQRES 3 B 219 GLU LEU LYS GLU THR LEU LEU LYS GLU LYS ARG ILE TYR
SEQRES 4 B 219 ILE ASP VAL PHE THR THR ARG PRO ASP THR VAL PHE GLY
SEQRES 5 B 219 ALA THR PHE VAL VAL LEU ALA PRO GLU HIS PRO LEU VAL
SEQRES 6 B 219 PRO VAL LEU ALA CYS ILE GLY GLU ARG LEU GLY ASN ALA
SEQRES 7 B 219 CYS TYR SER ASP VAL GLU ASN PHE VAL GLU LYS MET LYS
SEQRES 8 B 219 LYS MET SER THR ARG GLU ARG THR MET GLU GLU ASP LYS
SEQRES 9 B 219 GLU GLY VAL PHE LEU GLY VAL TYR ALA THR ASN PRO ALA
SEQRES 10 B 219 ASN GLY GLU LYS ILE PRO VAL TRP SER ALA ASN TYR VAL
SEQRES 11 B 219 LEU TYR GLU TYR GLY THR GLY ALA ILE MET CYS VAL PRO
SEQRES 12 B 219 ALA HIS ASP GLN ARG ASP TRP GLU PHE ALA LYS LYS TYR
SEQRES 13 B 219 ASP LEU PRO ILE LYS VAL VAL VAL LYS PRO GLU GLY ALA
SEQRES 14 B 219 TRP ASP PHE GLU LYS GLY ALA TYR GLU GLY LYS GLY THR
SEQRES 15 B 219 LEU VAL ASN SER ASP GLY PHE ASP GLY LEU ASP SER GLU
SEQRES 16 B 219 THR ALA LYS ARG LYS ILE THR GLU TRP LEU GLN ASP ARG
SEQRES 17 B 219 GLY LEU GLY GLU LYS LYS VAL SER TYR ARG LEU
FORMUL 3 HOH *513(H2 O)
HELIX 1 1 GLU A 240 VAL A 248 5 9
HELIX 2 2 PRO A 249 LYS A 260 1 12
HELIX 3 3 ARG A 270 ALA A 277 5 8
HELIX 4 4 PRO A 287 LEU A 299 1 13
HELIX 5 5 CYS A 303 LYS A 316 1 14
HELIX 6 6 SER A 318 MET A 324 1 7
HELIX 7 7 ASP A 370 ASP A 381 1 12
HELIX 8 8 SER A 410 ASP A 414 5 5
HELIX 9 9 ASP A 417 ARG A 432 1 16
HELIX 10 10 GLU B 240 VAL B 248 5 9
HELIX 11 11 PRO B 249 LYS B 260 1 12
HELIX 12 12 ARG B 270 ALA B 277 5 8
HELIX 13 13 PRO B 287 LEU B 299 1 13
HELIX 14 14 CYS B 303 LYS B 316 1 14
HELIX 15 15 SER B 318 MET B 324 1 7
HELIX 16 16 ASP B 370 ASP B 381 1 12
HELIX 17 17 SER B 410 ASP B 414 5 5
HELIX 18 18 ASP B 417 ARG B 432 1 16
SHEET 1 A 3 ARG A 261 THR A 268 0
SHEET 2 A 3 ALA A 230 GLU A 237 -1 N VAL A 236 O ILE A 262
SHEET 3 A 3 GLY A 435 LYS A 437 -1 O GLU A 436 N LEU A 231
SHEET 1 B 4 GLY A 330 THR A 338 0
SHEET 2 B 4 LYS A 345 ALA A 351 -1 O ILE A 346 N ALA A 337
SHEET 3 B 4 PHE A 279 LEU A 282 1 N VAL A 280 O TRP A 349
SHEET 4 B 4 ALA A 362 CYS A 365 -1 O CYS A 365 N PHE A 279
SHEET 1 C 2 VAL A 388 LYS A 389 0
SHEET 2 C 2 THR A 406 LEU A 407 -1 O THR A 406 N LYS A 389
SHEET 1 D 3 ARG B 261 THR B 268 0
SHEET 2 D 3 GLY B 229 GLU B 237 -1 N VAL B 236 O ILE B 262
SHEET 3 D 3 GLY B 435 LYS B 438 -1 O GLU B 436 N LEU B 231
SHEET 1 E 4 GLY B 330 THR B 338 0
SHEET 2 E 4 LYS B 345 ALA B 351 -1 O ILE B 346 N ALA B 337
SHEET 3 E 4 PHE B 279 LEU B 282 1 N VAL B 280 O TRP B 349
SHEET 4 E 4 ALA B 362 CYS B 365 -1 O ILE B 363 N VAL B 281
SHEET 1 F 2 VAL B 388 LYS B 389 0
SHEET 2 F 2 THR B 406 LEU B 407 -1 O THR B 406 N LYS B 389
SSBOND 1 CYS A 247 CYS A 294 1555 1555 2.11
SSBOND 2 CYS A 303 CYS B 303 1555 2675 2.39
SSBOND 3 CYS B 247 CYS B 294 1555 1555 2.08
CRYST1 38.689 98.180 116.667 90.00 90.00 90.00 P 21 21 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.025847 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010185 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008571 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
